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tmRNA to the rescue Structural motives for the salvage of stalled ribosomes

Lindahl, Martin LU (2010) In RNA Biology 7(5). p.577-581
Abstract
During translation, mRNA molecules are incidentally damaged, leaving the ribosome unable to reach or recognize the stop codon and thus stalled with mRNA and a potentially harmful polypeptide product attached to tRNA in the ribosomal P-site. In bacteria, a process called trans-translation has evolved, where a protein-RNA complex (smpB-tmRNA) mimicks the role of aminoacyl charged tRNA in the ribosomal A-site. The ribosome then resumes protein synthesis guided by an mRNA-like portion of the tmRNA which ends with a stop codon and codes for a peptide sequence susceptible to proteolysis, thus allowing the bacteria to salvage stalled ribosomes and degrade ill-defined and potentially harmful protein products. In this article, we will recollect how... (More)
During translation, mRNA molecules are incidentally damaged, leaving the ribosome unable to reach or recognize the stop codon and thus stalled with mRNA and a potentially harmful polypeptide product attached to tRNA in the ribosomal P-site. In bacteria, a process called trans-translation has evolved, where a protein-RNA complex (smpB-tmRNA) mimicks the role of aminoacyl charged tRNA in the ribosomal A-site. The ribosome then resumes protein synthesis guided by an mRNA-like portion of the tmRNA which ends with a stop codon and codes for a peptide sequence susceptible to proteolysis, thus allowing the bacteria to salvage stalled ribosomes and degrade ill-defined and potentially harmful protein products. In this article, we will recollect how structural studies have yielded a model for how the pre-translocation stages of trans-translation employing structural mimicry. We will also discuss possible models for (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
trans-translation, tmRNA, SmpB, cryo electron microscopy, single, particle, heterogeneity analysis
in
RNA Biology
volume
7
issue
5
pages
577 - 581
publisher
Taylor & Francis
external identifiers
  • wos:000288456500013
  • scopus:78649368975
ISSN
1547-6286
DOI
10.4161/rna.7.5.13214
language
English
LU publication?
yes
id
552cd1ce-1d0f-48bd-b3b5-48669a59982b (old id 1918195)
date added to LUP
2011-05-03 08:19:51
date last changed
2018-05-29 11:21:01
@misc{552cd1ce-1d0f-48bd-b3b5-48669a59982b,
  abstract     = {During translation, mRNA molecules are incidentally damaged, leaving the ribosome unable to reach or recognize the stop codon and thus stalled with mRNA and a potentially harmful polypeptide product attached to tRNA in the ribosomal P-site. In bacteria, a process called trans-translation has evolved, where a protein-RNA complex (smpB-tmRNA) mimicks the role of aminoacyl charged tRNA in the ribosomal A-site. The ribosome then resumes protein synthesis guided by an mRNA-like portion of the tmRNA which ends with a stop codon and codes for a peptide sequence susceptible to proteolysis, thus allowing the bacteria to salvage stalled ribosomes and degrade ill-defined and potentially harmful protein products. In this article, we will recollect how structural studies have yielded a model for how the pre-translocation stages of trans-translation employing structural mimicry. We will also discuss possible models for},
  author       = {Lindahl, Martin},
  issn         = {1547-6286},
  keyword      = {trans-translation,tmRNA,SmpB,cryo electron microscopy,single,particle,heterogeneity analysis},
  language     = {eng},
  number       = {5},
  pages        = {577--581},
  publisher    = {Taylor & Francis},
  series       = {RNA Biology},
  title        = {tmRNA to the rescue Structural motives for the salvage of stalled ribosomes},
  url          = {http://dx.doi.org/10.4161/rna.7.5.13214},
  volume       = {7},
  year         = {2010},
}